SU575353A1 - Method of obtaining carboxypepiidase - Google Patents
Method of obtaining carboxypepiidaseInfo
- Publication number
- SU575353A1 SU575353A1 SU7602318310A SU2318310A SU575353A1 SU 575353 A1 SU575353 A1 SU 575353A1 SU 7602318310 A SU7602318310 A SU 7602318310A SU 2318310 A SU2318310 A SU 2318310A SU 575353 A1 SU575353 A1 SU 575353A1
- Authority
- SU
- USSR - Soviet Union
- Prior art keywords
- acetate
- protein
- calcium
- buffer containing
- ammonium sulfate
- Prior art date
Links
Landscapes
- Enzymes And Modification Thereof (AREA)
Description
1one
Изобретеиие относитс к способу получени протеолитйческог о фермеита карбоксипептндаэы (КФ 3.4.12), примен емой в пищевой, текстильной и медицинской промывшейиости, а также в научной и лабораторной практике.The invention relates to a method for producing a proteolytic fermoite carboxypeptindaea (EC 3.4.12) used in food, textile and medical washing, as well as in scientific and laboratory practice.
В промышленном масштабе карбоксипептидаэу получают из сырь животного происхождени - поджелудочной железы крупного рогатого скота - путем многостадийной очистки и выделени фракции, содержащей карбоксипептидазу. В результате получают суспензию фермента, весьма нестойкую при хранении.On an industrial scale, carboxypeptidae is obtained from animal raw materials - the bovine pancreas - by multistage purification and separation of the fraction containing carboxypeptidase. The result is a suspension of the enzyme, very unstable during storage.
В насто щее врем наиболее перспе тивн1 О4И вл ютс - способы получени ферментов из микробных источников дешевого сырь и мощного продуцента ферментов со специфическими свойствамиCurrently, the most promising O4I are methods for producing enzymes from microbial sources of cheap raw materials and a powerful producer of enzymes with specific properties.
Одним из таких способов вл етс получение карбоксипептидазиой фракции из проназы - ферментного комплекса актиномицета Streptomyce&grisetis (str . ) путем осаждени белков сол ми , например сульфатом дк 1они , и органическими растворител ми, фракционировани белков на ионообменных смолах и молекул рных ситах с выделением смеси ферментов, вход щих в состав One such method is to obtain the carboxypeptidase fraction from the pronase – enzyme complex of Streptomyce & grisetis (Str.) Actinomycete by precipitating proteins with salts, for example dimethyl sulphate, and organic solvents, fractioning proteins on ion exchange resins and molecular sieves with separation of the mixture enzymes that are part of
проназы, и кх хроматографировани на колонке с амберлитом.pronase, and kx chromatography on an amberlite column.
Белок карбоксипептидазной фракции осаждают из раствора сульфатом ак юни , осадок раствор ют в буфере и лл лее диализуют с получением фермеита в виде раствора.The protein of the carboxypeptidase fraction is precipitated from the solution by sulphate of akuni, the precipitate is dissolved in a buffer and then dialyzed to obtain fermitic in the form of a solution.
К недостаткам известного способа относ тс низкий выход целевого продукта и получение фермеита с ииэкими| удельными активностью и стабильность при хранении.The disadvantages of this method include the low yield of the target product and the production of a fermitite with iekimi | specific activity and storage stability.
Цель изобретени - повышение стабильности фермента, его удельной активности и выхода - достигаетс тем, tTO из культуральной жидкости актинов мидета Str. fHeeus после фильтровани осаждают белки добавлением сульфата аммони до полного насыщени , а полученную после диализа карбоксипепг тидазу лиофилизируют в ацетатном буфере , содержащем ионы кальци , предпочтительно в 0,05 М ацетатном буфере , содержащем 0,01 М ацетат кальци The purpose of the invention is to increase the stability of the enzyme, its specific activity and yield - by tTO from the culture fluid of actin midin Str. After filtration, the fHeeus precipitates the proteins by adding ammonium sulfate until complete saturation, and the carboxypepididase obtained after dialysis is lyophilized in acetate buffer containing calcium ions, preferably in 0.05 M acetate buffer containing 0.01 M calcium acetate
Claims (2)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SU7602318310A SU575353A1 (en) | 1976-01-22 | 1976-01-22 | Method of obtaining carboxypepiidase |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
SU7602318310A SU575353A1 (en) | 1976-01-22 | 1976-01-22 | Method of obtaining carboxypepiidase |
Publications (1)
Publication Number | Publication Date |
---|---|
SU575353A1 true SU575353A1 (en) | 1977-10-05 |
Family
ID=20646908
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SU7602318310A SU575353A1 (en) | 1976-01-22 | 1976-01-22 | Method of obtaining carboxypepiidase |
Country Status (1)
Country | Link |
---|---|
SU (1) | SU575353A1 (en) |
-
1976
- 1976-01-22 SU SU7602318310A patent/SU575353A1/en active
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Morse et al. | A new approach to the study of urinary macromolecules as a participant in calcium oxalate crystallization | |
Tager | Concentration, partial purification, properties, and nature of staphylocoagulase | |
CN112724242B (en) | Method for producing recombinant human-like collagen and host cell protein by using pichia pastoris | |
SU1012786A3 (en) | Method for preparing proteinaceous complex stimulating secretion of insulin | |
CN101104635A (en) | Method for purifying recombination human alpha-whey albumin from transgene cow milk | |
SU575353A1 (en) | Method of obtaining carboxypepiidase | |
Berridge et al. | 516. A simple method for preparing crystalline rennin | |
DE1292609B (en) | Process for the production and recovery of lipoprotein lipase by culturing microorganisms | |
Richardson et al. | The phosphoprotein of rabbit incisors | |
US4027012A (en) | Process for the extraction of components having anticoagulant activity "in vivo" from snake venoms and products obtained | |
EP1306383B1 (en) | Method of purifying a calcium ion-binding protein | |
US4960756A (en) | Lectin like protein substance, method of obtaining same and anti-tumor agent comprising same | |
SU535912A3 (en) | Method of producing orgotein | |
SU1280546A1 (en) | Method of producing leukocytic beta sub 1 - glycoproteide | |
SU411867A1 (en) | ||
SU1487817A3 (en) | Method of extracting carboxypeptidase b from adrenal gland of mammals | |
SU508509A1 (en) | Method for isolating enzymes of microbial bee mass | |
EP0042560A2 (en) | A process for producing and obtaining anaphylatoxin- and cocytotaxin-containing leucotaxine preparations and of anaphylatoxin and cocytotaxin proteins in molecularly homogeneous, biologically active form | |
Lundblad et al. | Purification of cathepsin B from oocytes and mature eggs of the sea urchin Brissopsis lyrifera by means of gel filtration | |
SU1655987A1 (en) | Method for preparation of purified neuraminidase of choleric vibrio | |
SE7506666L (en) | PROCEDURE FOR CULTIVATION OF FOODS-ENCELLS PROTEINS WHILE EXTENSIVE ACTIVE SUBSTANCES FROM THE WATER. | |
RU2175195C1 (en) | Method of isolating anigiogenin-rich protein fraction | |
RU2634408C1 (en) | Method for production of active pharmaceutical substance of recombinant bismetionilystone h1.3 | |
RU1526226C (en) | Method of obtaining collagenaze | |
SU1223913A1 (en) | Method of obtaining galactosidase |